1ksr
From Proteopedia
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'''THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION FACTOR (ABP-120) HAVE AN IMMUNOGLOBULIN FOLD, NMR, 20 STRUCTURES''' | '''THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION FACTOR (ABP-120) HAVE AN IMMUNOGLOBULIN FOLD, NMR, 20 STRUCTURES''' | ||
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[[Category: Noegel, A A.]] | [[Category: Noegel, A A.]] | ||
[[Category: Renner, C.]] | [[Category: Renner, C.]] | ||
| - | [[Category: | + | [[Category: Abp-120]] |
| - | [[Category: | + | [[Category: Actin binding protein]] |
| - | [[Category: | + | [[Category: Gelation factor]] |
| - | [[Category: | + | [[Category: Immunoglobulin]] |
| - | [[Category: | + | [[Category: Structure]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:07:38 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:07, 2 May 2008
THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION FACTOR (ABP-120) HAVE AN IMMUNOGLOBULIN FOLD, NMR, 20 STRUCTURES
Overview
The 120,000 M(r) gelation factor and alpha-actinin are among the most abundant F-actin cross-linking proteins in Dictyostelium discoideum. Both molecules are rod-shaped homodimers. Each monomer chain is comprised of an actin-binding domain and a rod domain. The rod domain of the gelation factor consists of six 100-residue repetitive segments with high internal homology. We have now determined the three-dimensional structure of segment 4 of the rod domain of the gelation factor from D. discoideum using NMR spectroscopy. The segment consists of seven beta-sheets arranged in an immunoglobulin-like (Ig) fold. This is completely different from the alpha-actinin rod domain which consists of four spectrin-like alpha-helical segments. The gelation factor is the first example of an Ig-fold found in an actin-binding protein. Two highly homologous actin-binding proteins from human with similar sequences to the gelation factor, filamin and a 280,000 M(r) actin-binding protein (ABP-280), share conserved residues that form the core of the gelation factor repetitive segment structure. Thus, the segment 4 structure should be common to this subfamily of the spectrin superfamily. The structure of segment 4 together with previously published electron microscopy data, provide an explanation for the dimerization of the whole gelation factor molecule.
About this Structure
1KSR is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.
Reference
The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold., Fucini P, Renner C, Herberhold C, Noegel AA, Holak TA, Nat Struct Biol. 1997 Mar;4(3):223-30. PMID:9164464 Page seeded by OCA on Fri May 2 23:07:38 2008
